Method for inhibition of pathogenic microorganisms

a technology for pathogenic microorganisms and inhibitors, which is applied in the direction of peptide sources, applications, genetic material ingredients, etc., can solve the problems of few reports of primary human macrophage transfection with dna plasmids, insufficient yield of recombinant methods, etc., and achieve the effect of inhibiting preventing the growth of a microorganism

Inactive Publication Date: 2006-05-25
UNIV OF MEDICINE & DENTISTRY OF NEW JERSEY +1
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The present invention relates to a method for inhibiting the growth of microorganisms in a human cell. The method involves transfecting the human cell with a nucleic acid encoding a therapeutic protein, such as a defensin, using a liposome delivery vehicle. The therapeutic protein is expressed by the human cell and inhibits the growth of the microorganism. The method can be used to treat diseases caused by pathogenic microorganisms in humans.

Problems solved by technology

Although defensins have been proposed for use as therapeutics (Ganz and Lehrer, Pharmacology &Therapeutics 66:191-205, 1995), chemical synthesis of these peptides is a challenge due to the complex pattern of disulfide bonds which stabilize the structure (Lauth et al., Insect Biochem Mol Biol 28:1059-66, 1998), and recombinant methods do not produce sufficient yields (Harwig et al., Meth. in Enzymol.
To date, however, there are very few reports of primary human macrophage transfection with DNA plasmids.

Method used

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Examples

Experimental program
Comparison scheme
Effect test

example 1

[0081] The following example describes the optimization of transfection efficiency for transfection of mRNA into macrophages using enhanced green fluorescent protein (eGFP).

[0082] Monocytes were isolated from human whole blood by centrifugation through Ficoll-Hypaque. The mononuclear cell layer was washed in RPMI 1640+saline, and the monocytes counted. Approximately 1×106 monocytes were dispensed into the wells of 24 well plates (Falcon, Becton Dickinson), and allowed to adhere for one hour. The monolayers were then washed three times to remove non-adherent cells. The resulting cell monolayers consisted of M. tuberculosis (Erdman). Cells were placed at 100,000 / well into 8 well chambered coverslips (Nalge-Nunc intl., Naperville, Ill.) and allowed to adhere for 2 hours in RPMI1640 including penicillin (0.05 units / ml), streptomycin (0.05 μg / ml), L-glutamine, and 10% autologous human serum. Non-adherent cells were then removed with 3 washes with warm PBS, and the medium replaced with a...

example 2

[0090] The following example demonstrates the relative toxicities of mRNAs encoding GFP vs hBD-2.

[0091] Cationic lipids are known to be toxic to mammalian cells at high concentration (Freedland et al., Biochem Mol Med 59:144-53, 1996), as are defensins (Lichtenstein et al., Blood 68:1407-1410, 1986). The present inventors therefore sought to determine the maximum dose of GFP mRNA / oligofectin G complex which could be applied to the macrophages, and whether human β-defensin (hBD-2) mRNA had greater toxicity. Specifically, the inventors determined the ability of human monocyte-derived macrophages (MDM) to reduce MTT 24 hours after treatment with increasing concentrations of either GFP mRNA (produced as described in Example 1) or hBD-2 mRNA (see below) complexed with Oligofectin G.

[0092] hBD-2 cDNA was produced by RT-PCR using human tracheal epithelial cell mRNA as a template and published primer sequences (Harder et al., Nature 387:861, 1997, incorporated herein by reference in its e...

example 3

[0094] The following example demonstrates the production of hBD-2, and association with intracellular M. tuberculosis following mRNA transfection.

[0095] It was thought that the ability of hBD-2 to affect the growth of M. tuberculosis within macrophages would depend in part on the ability of the defensin protein to gain access to the mycobacteria. Therefore, immunocytochemistry was performed using a specific rabbit anti-human hBD-2 antiserum to determine if hBD-2 protein was produced following transfection of macrophages with hBD-2 mRNA, and to determine where in the macrophages the protein localized.

[0096] For immunocytochemistry, cells were grown on eight chamber slides, fixed in formalin at 4° C., and washed in 1M glycine. Immunohistochemistry was carried out as described (Yount et al., J Biol Chem 274:26249-58, 1999), using specific hBD-2 antibody (a gift of T. Ganz) or non-immune serum, and visualized using the Vector ABC kit (Vectorlabs). Acid-fast staining of mycobacteria wa...

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Abstract

Disclosed is a method for inhibiting the growth of a microorganism by high efficiency transfection of a human host cell with a nucleic acid encoding an antimicrobial agent, such that the host cell expresses the antimicrobial agent effective to inhibit growth of the microorganism.

Description

CROSS-REFERENCE TO RELATED APPLICATIONS [0001] This application claims priority under 35 U.S.C. § 119(e) from U.S. Provisional Application Ser. No. 60 / 157,348, filed on Sep. 30, 1999, and entitled “A novel anti-mycobacterial agent based on mRNA encoding human β-defensin 2 enables primary macrophages to restrict growth of Mycobacterium tuberculosis.” The entire disclosure of U.S. Provisional Application Ser. No. 60 / 157,348 is incorporated herein by reference.GOVERNMENT RIGHTS [0002] This invention was made in part with government support under NIH Grant HL53400, awarded by the National Institutes of Health. The government has certain rights to this invention.FIELD OF THE INVENTION [0003] This invention generally relates to a method for producing a therapeutic protein in a human host cell, and particularly, in a human primary macrophage. The invention also relates to a method to inhibit the growth of a pathogenic microorganism by expressing such a therapeutic protein in a human host c...

Claims

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Application Information

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Patent Type & AuthorityApplications(United States)
IPC IPC(8): A61K48/00A61K9/127C12N15/88C07K14/47C12N5/08
CPCA61K9/127A61K48/00A61K48/0025A61K48/005C07K14/4723Y02A50/30
InventorKISICH, KEVINDIAMOND, GILL
OwnerUNIV OF MEDICINE & DENTISTRY OF NEW JERSEY